Proteomics 2013, 13, 3387–3392
DOI 10.1002/pmic.201300131
3387
TECHNICAL BRIEF
Facile synthesis of magnetic metal organic frameworks for the enrichment of low-abundance peptides for MALDI-TOF MS analysis Man Zhao, Chunhui Deng, Xiangmin Zhang and Pengyuan Yang Department of Chemistry, Fudan University, Shanghai, China
In this work, core-shell magnetic metal organic framework (MOF) microspheres were successfully synthesized by coating magnetite particles with mercaptoacetic acid and subsequent reactions with ethanol solutions of Cu(OAc)2 and benzene-1,3,5-tricarboxylic acid (designated as H3 btc) alternately. The resulting Fe3 O4 @[Cu3 (btc)2 ] possess strong magnetic responsiveness. We applied the novel nanocomposites in the enrichment of low-concentration standard peptides, peptides in MYO and BSA tryptic digests and in human urine in combination with MALDI-TOF MS analysis for the first time. In addition, the Cu3 (btc)2 MOF shells exhibit strong affinity to peptides, thus providing a rapid and convenient approach to the concentration of low-abundance peptides. Notably, peptides at an extremely low concentration of 10 pM could be detected by MALDI-TOF MS after enrichment with the magnetic MOF composites. In brief, the facile synthesis and efficient enrichment process of the Fe3 O4 @[Cu3 (btc)2 ] microspheres make them promising candidates for the isolation of peptides in even complex biological environments.
Received: March 30, 2013 Revised: September 5, 2013 Accepted: October 11, 2013
Keywords: Enrichment / Low-abundance peptides / Magnetic MOFs microspheres / MALDI-TOF MS / Nanoproteomics
Additional supporting information may be found in the online version of this article at the publisher’s web-site
Since MALDI technique was developed by Tanaka and Karas in the late 1980s’ and was combined with TOF MS as a detection platform, MALDI-TOF MS along with database searching has become a major and indispensable analytical approach for proteomics research [1–3]. Though MALDITOF MS is highly sensitive to trace amounts of peptides or proteins, it appears to be insufficient for the detection of low-abundance peptides/proteins that exist in real biological samples. Since these peptides/proteins are not only of extremely low concentrations (
DOI 10.1002/pmic.201300131
3387
TECHNICAL BRIEF
Facile synthesis of magnetic metal organic frameworks for the enrichment of low-abundance peptides for MALDI-TOF MS analysis Man Zhao, Chunhui Deng, Xiangmin Zhang and Pengyuan Yang Department of Chemistry, Fudan University, Shanghai, China
In this work, core-shell magnetic metal organic framework (MOF) microspheres were successfully synthesized by coating magnetite particles with mercaptoacetic acid and subsequent reactions with ethanol solutions of Cu(OAc)2 and benzene-1,3,5-tricarboxylic acid (designated as H3 btc) alternately. The resulting Fe3 O4 @[Cu3 (btc)2 ] possess strong magnetic responsiveness. We applied the novel nanocomposites in the enrichment of low-concentration standard peptides, peptides in MYO and BSA tryptic digests and in human urine in combination with MALDI-TOF MS analysis for the first time. In addition, the Cu3 (btc)2 MOF shells exhibit strong affinity to peptides, thus providing a rapid and convenient approach to the concentration of low-abundance peptides. Notably, peptides at an extremely low concentration of 10 pM could be detected by MALDI-TOF MS after enrichment with the magnetic MOF composites. In brief, the facile synthesis and efficient enrichment process of the Fe3 O4 @[Cu3 (btc)2 ] microspheres make them promising candidates for the isolation of peptides in even complex biological environments.
Received: March 30, 2013 Revised: September 5, 2013 Accepted: October 11, 2013
Keywords: Enrichment / Low-abundance peptides / Magnetic MOFs microspheres / MALDI-TOF MS / Nanoproteomics
Additional supporting information may be found in the online version of this article at the publisher’s web-site
Since MALDI technique was developed by Tanaka and Karas in the late 1980s’ and was combined with TOF MS as a detection platform, MALDI-TOF MS along with database searching has become a major and indispensable analytical approach for proteomics research [1–3]. Though MALDITOF MS is highly sensitive to trace amounts of peptides or proteins, it appears to be insufficient for the detection of low-abundance peptides/proteins that exist in real biological samples. Since these peptides/proteins are not only of extremely low concentrations (
